Synthesis of a mixed disulfide of egg white lysozyme and glutathione ‐ a model substrate for enzymatic reduction of protein mixed disulfides

Axelsson, Kent; Mannervik, Bengt

doi:10.1016/0014-5793(75)80677-6

Cited by 15 publications

(2 citation statements)

References 16 publications

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“…This result shows that glutathione reductase in rat liver cannot directly reduce the lysozyme derivative (or Cys (SO3H)]. This statement is supported by previous experiments with highly purified glutathione reductase from rat liver and from yeast (Axelsson & Mannervik, 1975). A still more important finding was that the thioltransferase activity obtained with the mixed disulphide of lysozyme and GSH coincided with the enzymic activity previously found with low-molecular-weight disulphides and thiosulphate esters [including Cys(SO3H) (Eriksson & Mannervik, 1970;].…”

Section: Resultssupporting

confidence: 81%

See 1 more Smart Citation

Reduction of disulphide bonds in proteins mixed disulphides catalysed by a thioltransferase in rat liver cytosol

Mannervik

Axelsson

1975

Biochemical Journal

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The reduction of mixed disulphides of some proteins and GSH [Protein(-SSG)n] is accomplished with GSH as a reductant and a thioltransferase from rat liver as a catalyst, thus: See article. The spontaneous reaction is negligible in comparison with the enzymic reaction in vivo, and any direct reduction with glutathione reductase is not detectable with the substrates used. The reduction is only indirectly dependent on NADPH, which is required for the regeneration of GSH from GSSG. Other protein disulphides apparently are reduced via analogous GSH-dependent reactions

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Section: Resultssupporting

confidence: 81%

“…The synthesis of a mixed disulphide of egg-white lysozyme and GSH was described in a recent paper from this laboratory (Axelsson & Mannervik, 1975). S-Sulphocysteine [Cys(SO3H)] was synthesized as described by Segel & Johnson (1963).…”

Section: Methodsmentioning

confidence: 99%